TDP-43 Is Intrinsically Aggregation-prone, and Amyotrophic Lateral Sclerosis-linked Mutations Accelerate Aggregation and Increase Toxicity

Non-amyloid, ubiquitinated cytoplasmic inclusions containing TDP-43 and its C-terminal fragments are pathological hallmarks of amyotrophic lateral sclerosis (ALS), a fatal motor neuron disorder, and frontotemporal lobar degeneration with ubiquitin-positive inclusions (FTLD-U). Importantly, TDP-43 mu...

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Veröffentlicht in:	The Journal of biological chemistry 2009-07, Vol.284 (30), p.20329-20339
Hauptverfasser:	Johnson, Brian S., Snead, David, Lee, Jonathan J., McCaffery, J. Michael, Shorter, James, Gitler, Aaron D.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amyotrophic Lateral Sclerosis - pathology DNA-Binding Proteins - chemistry DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism Humans Molecular Basis of Cell and Developmental Biology Mutagenesis, Site-Directed Mutant Proteins - chemistry Mutant Proteins - genetics Mutant Proteins - metabolism Neurons - pathology Protein Folding Protein Structure, Tertiary Saccharomyces cerevisiae - genetics
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